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Enoyl-[acyl-carrier-protein] reductase [NADH] (ENR) (EC 1.3.1.9)

 FABV_YERPE              Reviewed;         399 AA.
Q8Z9U1; Q0W9T3; Q74PB4; Q7CFN5;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000303|PubMed:22244758};
Short=ENR {ECO:0000303|PubMed:22244758};
EC=1.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01838};
Name=fabV {ECO:0000303|PubMed:22244758};
OrderedLocusNames=YPO4104, y4119, YP_4011;
Yersinia pestis.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Yersiniaceae; Yersinia.
NCBI_TaxID=632;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CO-92 / Biovar Orientalis;
PubMed=11586360; DOI=10.1038/35097083;
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
"Genome sequence of Yersinia pestis, the causative agent of plague.";
Nature 413:523-527(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KIM10+ / Biovar Mediaevalis;
PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C.,
Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
Perry R.D.;
"Genome sequence of Yersinia pestis KIM.";
J. Bacteriol. 184:4601-4611(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=91001 / Biovar Mediaevalis;
PubMed=15368893; DOI=10.1093/dnares/11.3.179;
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z.,
Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
Yang H., Wang J., Huang P., Yang R.;
"Complete genome sequence of Yersinia pestis strain 91001, an isolate
avirulent to humans.";
DNA Res. 11:179-197(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG AND NAD, FUNCTION, ENZYME REGULATION, AND SUBUNIT.
PubMed=22244758; DOI=10.1016/j.str.2011.07.019;
Hirschbeck M.W., Kuper J., Lu H., Liu N., Neckles C., Shah S.,
Wagner S., Sotriffer C.A., Tonge P.J., Kisker C.;
"Structure of the Yersinia pestis FabV enoyl-ACP reductase and its
interaction with two 2-pyridone inhibitors.";
Structure 20:89-100(2012).
[5]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NAD.
Neckles C., Hirschbeck M.W., Shah S., Pan P., Bommineni G.R., Yu W.,
Liu N., Davoodi S., Kisker C., Tonge P.J.;
"Enoyl-ACP reductase from Yersinia pestis (wildtype) with cofactor
NADH.";
Submitted (APR-2013) to the PDB data bank.
-!- FUNCTION: Involved in the final reduction of the elongation cycle
of fatty acid synthesis (FAS II). Catalyzes the reduction of a
carbon-carbon double bond in an enoyl moiety that is covalently
linked to an acyl carrier protein (ACP).
{ECO:0000269|PubMed:22244758}.
-!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
{ECO:0000255|HAMAP-Rule:MF_01838}.
-!- ENZYME REGULATION: Inhibited by 2-pyridone derivatives such as
PT172 and PT173. {ECO:0000269|PubMed:22244758}.
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22244758}.
-!- SIMILARITY: Belongs to the TER reductase family.
{ECO:0000255|HAMAP-Rule:MF_01838}.
-----------------------------------------------------------------------
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EMBL; AL590842; CAL22672.1; -; Genomic_DNA.
EMBL; AE009952; AAM87661.1; -; Genomic_DNA.
EMBL; AE017042; AAS64150.1; -; Genomic_DNA.
PIR; AD0498; AD0498.
RefSeq; WP_002215588.1; NZ_LT605018.1.
RefSeq; YP_002348955.1; NC_003143.1.
PDB; 3ZU2; X-ray; 2.10 A; A=1-399.
PDB; 3ZU3; X-ray; 1.80 A; A=1-399.
PDB; 3ZU4; X-ray; 2.01 A; A=1-399.
PDB; 3ZU5; X-ray; 2.00 A; A=1-399.
PDB; 4BKQ; X-ray; 2.30 A; A=1-399.
PDB; 5JAI; X-ray; 1.90 A; A=1-399.
PDB; 5JAM; X-ray; 2.00 A; A=1-399.
PDB; 5JAQ; X-ray; 1.90 A; A=1-399.
PDBsum; 3ZU2; -.
PDBsum; 3ZU3; -.
PDBsum; 3ZU4; -.
PDBsum; 3ZU5; -.
PDBsum; 4BKQ; -.
PDBsum; 5JAI; -.
PDBsum; 5JAM; -.
PDBsum; 5JAQ; -.
ProteinModelPortal; Q8Z9U1; -.
SMR; Q8Z9U1; -.
IntAct; Q8Z9U1; 2.
STRING; 187410.y4119; -.
BindingDB; Q8Z9U1; -.
PRIDE; Q8Z9U1; -.
DNASU; 1149066; -.
EnsemblBacteria; AAM87661; AAM87661; y4119.
EnsemblBacteria; AAS64150; AAS64150; YP_4011.
GeneID; 1176932; -.
KEGG; ype:YPO4104; -.
KEGG; ypk:y4119; -.
KEGG; ypm:YP_4011; -.
PATRIC; fig|214092.21.peg.4646; -.
eggNOG; ENOG4105RKW; Bacteria.
eggNOG; COG3007; LUCA.
HOGENOM; HOG000269390; -.
KO; K00209; -.
BRENDA; 1.3.1.9; 4559.
UniPathway; UPA00094; -.
Proteomes; UP000000815; Chromosome.
Proteomes; UP000001019; Chromosome.
Proteomes; UP000002490; Chromosome.
GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
HAMAP; MF_01838; FabV_reductase; 1.
InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
PANTHER; PTHR37480; PTHR37480; 1.
Pfam; PF07055; Eno-Rase_FAD_bd; 1.
Pfam; PF12242; Eno-Rase_NADH_b; 1.
Pfam; PF12241; Enoyl_reductase; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NAD;
Oxidoreductase; Reference proteome.
CHAIN 1 399 Enoyl-[acyl-carrier-protein] reductase
[NADH].
/FTId=PRO_0000220063.
NP_BIND 48 53 NAD. {ECO:0000269|PubMed:22244758,
ECO:0000269|Ref.5}.
NP_BIND 74 75 NAD. {ECO:0000269|PubMed:22244758,
ECO:0000269|Ref.5}.
NP_BIND 111 112 NAD. {ECO:0000269|PubMed:22244758,
ECO:0000269|Ref.5}.
NP_BIND 139 140 NAD. {ECO:0000255|HAMAP-Rule:MF_01838}.
NP_BIND 274 276 NAD. {ECO:0000269|PubMed:22244758,
ECO:0000269|Ref.5}.
ACT_SITE 235 235 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_01838,
ECO:0000305|PubMed:22244758}.
BINDING 225 225 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01838}.
BINDING 244 244 NAD. {ECO:0000269|PubMed:22244758,
ECO:0000269|Ref.5}.
SITE 75 75 Plays an important role in discriminating
NADH against NADPH. {ECO:0000255|HAMAP-
Rule:MF_01838}.
CONFLICT 233 233 D -> Y (in Ref. 3; AAS64150).
{ECO:0000305}.
STRAND 11 13 {ECO:0000244|PDB:3ZU2}.
HELIX 17 34 {ECO:0000244|PDB:3ZU3}.
STRAND 42 48 {ECO:0000244|PDB:3ZU3}.
HELIX 52 65 {ECO:0000244|PDB:3ZU3}.
STRAND 68 73 {ECO:0000244|PDB:3ZU3}.
HELIX 86 100 {ECO:0000244|PDB:3ZU3}.
STRAND 105 110 {ECO:0000244|PDB:3ZU3}.
HELIX 115 128 {ECO:0000244|PDB:3ZU3}.
STRAND 132 137 {ECO:0000244|PDB:3ZU3}.
STRAND 142 145 {ECO:0000244|PDB:3ZU3}.
TURN 147 149 {ECO:0000244|PDB:3ZU3}.
STRAND 152 154 {ECO:0000244|PDB:3ZU3}.
STRAND 160 162 {ECO:0000244|PDB:3ZU3}.
STRAND 164 170 {ECO:0000244|PDB:3ZU3}.
TURN 171 174 {ECO:0000244|PDB:3ZU3}.
STRAND 175 181 {ECO:0000244|PDB:3ZU3}.
HELIX 186 196 {ECO:0000244|PDB:3ZU3}.
HELIX 199 211 {ECO:0000244|PDB:3ZU3}.
STRAND 214 224 {ECO:0000244|PDB:3ZU3}.
HELIX 229 231 {ECO:0000244|PDB:3ZU3}.
TURN 232 237 {ECO:0000244|PDB:3ZU3}.
HELIX 239 259 {ECO:0000244|PDB:3ZU3}.
TURN 260 262 {ECO:0000244|PDB:3ZU3}.
STRAND 265 270 {ECO:0000244|PDB:3ZU3}.
HELIX 277 280 {ECO:0000244|PDB:3ZU3}.
HELIX 285 299 {ECO:0000244|PDB:3ZU3}.
HELIX 305 315 {ECO:0000244|PDB:3ZU3}.
STRAND 318 320 {ECO:0000244|PDB:3ZU3}.
STRAND 328 331 {ECO:0000244|PDB:5JAM}.
HELIX 334 337 {ECO:0000244|PDB:3ZU3}.
HELIX 339 351 {ECO:0000244|PDB:3ZU3}.
TURN 354 356 {ECO:0000244|PDB:3ZU3}.
HELIX 357 360 {ECO:0000244|PDB:3ZU3}.
HELIX 363 373 {ECO:0000244|PDB:3ZU3}.
STRAND 396 398 {ECO:0000244|PDB:3ZU3}.
SEQUENCE 399 AA; 43346 MW; 860F449EF0C24895 CRC64;
MIIKPRVRGF ICVTAHPTGC EANVKKQIDY VTTEGPIANG PKRVLVIGAS TGYGLAARIT
AAFGCGADTL GVFFERPGEE GKPGTSGWYN SAAFHKFAAQ KGLYAKSING DAFSDEIKQL
TIDAIKQDLG QVDQVIYSLA SPRRTHPKTG EVFNSALKPI GNAVNLRGLD TDKEVIKESV
LQPATQSEID STVAVMGGED WQMWIDALLD AGVLAEGAQT TAFTYLGEKI THDIYWNGSI
GAAKKDLDQK VLAIRESLAA HGGGDARVSV LKAVVTQASS AIPMMPLYLS LLFKVMKEKG
THEGCIEQVY SLYKDSLCGD SPHMDQEGRL RADYKELDPE VQNQVQQLWD QVTNDNIYQL
TDFVGYKSEF LNLFGFGIDG VDYDADVNPD VKIPNLIQG


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